E
Ellinor I.B. Peerschke
Researcher at Memorial Sloan Kettering Cancer Center
Publications - 154
Citations - 7626
Ellinor I.B. Peerschke is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Platelet & Receptor. The author has an hindex of 44, co-authored 151 publications receiving 6770 citations. Previous affiliations of Ellinor I.B. Peerschke include University of Rochester & University of Debrecen.
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A murine monoclonal antibody that completely blocks the binding of fibrinogen to platelets produces a thrombasthenic-like state in normal platelets and binds to glycoproteins IIb and/or IIIa.
TL;DR: There is probably a single anatomic site that is crucial to the binding of all fibrinogen molecules and that this site is most likely on the glycoprotein IIb/IIIa complex, according to studies of a murine monoclonal antibody produced by the hybridoma technique.
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Guideline for Reversal of Antithrombotics in Intracranial Hemorrhage: A Statement for Healthcare Professionals from the Neurocritical Care Society and Society of Critical Care Medicine.
Jennifer A. Frontera,John J. Lewin,Alejandro A. Rabinstein,Imo P. Aisiku,Anne W. Alexandrov,Anne W. Alexandrov,Aaron M. Cook,Gregory J. del Zoppo,Monisha A. Kumar,Ellinor I.B. Peerschke,Michael F. Stiefel,Jeanne Teitelbaum,Katja E. Wartenberg,Cindy L. Zerfoss +13 more
TL;DR: This guideline provides timely, evidence-based reversal strategies to assist practitioners in the care of patients with antithrombotic-associated intracranial hemorrhage.
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Studies with a murine monoclonal antibody that abolishes ristocetin- induced binding of von Willebrand factor to platelets: additional evidence in support of GPIb as a platelet receptor for von Willebrand factor
TL;DR: Immunoprecipitation and affinity chromatography studies indicated that the antibody binds to glycoprotein lb at a site contained on the externally oriented portion of the GPIb alpha chain (glycocalicin).
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Senolytic CAR T cells reverse senescence-associated pathologies.
Corina Amor,Judith Feucht,Josef Leibold,Yu-Jui Ho,Changyu Zhu,Direna Alonso-Curbelo,Jorge Mansilla-Soto,Jacob A. Boyer,Xiang Li,Xiang Li,Theodoros Giavridis,Amanda Kulick,Shauna L. Houlihan,Ellinor I.B. Peerschke,Scott L. Friedman,Vladimir Ponomarev,Alessandra Piersigilli,Michel Sadelain,Scott W. Lowe,Scott W. Lowe +19 more
TL;DR: Chimeric antigen receptor (CAR) T cells targeting uPAR, a cell-surface protein that is upregulated on senescent cells, eliminate senescence cells in vitro and in vivo and reduce liver fibrosis in mice.
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Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q.
TL;DR: The "mature" protein, corresponding to amino acid residues 74-282 of the predicted pre-pro sequence, was overexpressed in Escherichia coli and was purified to homogeneity and was able to inhibit the complement-mediated lysis of sheep erythrocytes by human serum and was shown to be a tetramer by gel filtration in nondissociating conditions.